| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10536811 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2012 | 7 Pages |
Abstract
⺠The thermal and chemical stability of GthGT and its T353A mutant has been reported. ⺠An intermediate has been detected during the thermal unfolding of GthGT and T353A. ⺠Mature GthGT is more susceptible at acidic pH to chemical denaturation than T353A. ⺠Electrostatics are important for the stability of GthGT.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Andrea Pica, Irene Russo Krauss, Immacolata Castellano, Mosè Rossi, Francesco La Cara, Giuseppe Graziano, Filomena Sica, Antonello Merlino,